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Crystal structure of an iron superoxide dismutase from the pathogenic amoeba Acanthamoeba castellanii
Author(s) -
Dao Oanh,
Asaithambi Killivalavan,
Na Byeong Kuk,
Lee Kon Ho
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x19008112
Subject(s) - superoxide dismutase , escherichia coli , biology , effector , microbiology and biotechnology , superoxide , oxidative stress , biochemistry , chemistry , enzyme , gene
The iron superoxide dismutase found in the pathogenic amoeba Acanthamoeba castellanii ( Ac FeSOD) may play essential roles in the survival of the parasite, not only by protecting it from endogenous oxidative stress but also by detoxifying oxidative killing of the parasite by host immune effector cells. The Ac FeSOD protein was expressed in a stable form using an Escherichia coli expression system and was crystallized by the microbatch and hanging‐drop vapour‐diffusion methods. The structure was determined to 2.33 Å resolution from a single Ac FeSOD crystal. The crystal belonged to the hexagonal space group P 6 1 and contained 12 molecules forming three tetramers in the asymmetric unit, with an iron ion bound in each molecule. Structural comparisons and sequence alignment of Ac FeSOD with other FeSODs showed a well conserved overall fold and conserved active‐site residues with subtle differences.